Molecular Cloning, Chromosomal Localization, Tissue mRNA Levels, Bacterial Expression, and Enzymatic Properties of Human NMN Adenylyltransferase *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 276, Issue: 1, Page: 406-412
2001
- 143Citations
- 61Captures
- 3Mentions
Metric Options: Counts1 Year3 YearSelecting the 1-year or 3-year option will change the metrics count to percentiles, illustrating how an article or review compares to other articles or reviews within the selected time period in the same journal. Selecting the 1-year option compares the metrics against other articles/reviews that were also published in the same calendar year. Selecting the 3-year option compares the metrics against other articles/reviews that were also published in the same calendar year plus the two years prior.
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations143
- Citation Indexes143
- CrossRef143
- 127
- Captures61
- Readers61
- 61
- Mentions3
- References3
- Wikipedia3
Article Description
A 1329-base pair clone isolated from a human placenta cDNA library contains a full-length 837-base pair coding region for a 31.9-kDa protein whose deduced primary structure exhibits high homology to consensus sequences found in other NMN adenylyltransferases. Northern blotting detected a major 3.1-kilobase mRNA transcript as well as a minor 4.1-kilobase transcript in all human tissues examined. In several cancer cell lines, lower levels of mRNA expression were clearly evident. The gene encoding the human enzyme was mapped to chromosome band 1p32–35. High efficiency bacterial expression yielded 1.5 mg of recombinant enzyme/liter of culture medium. The molecular and kinetic properties of recombinant human NMN adenylyltransferase provide new directions for investigating metabolic pathways involving this enzyme.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925818442524; http://dx.doi.org/10.1074/jbc.m008700200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0035808313&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/11027696; https://linkinghub.elsevier.com/retrieve/pii/S0021925818442524; http://www.jbc.org/lookup/doi/10.1074/jbc.M008700200; https://syndication.highwire.org/content/doi/10.1074/jbc.M008700200; https://dx.doi.org/10.1074/jbc.m008700200
Elsevier BV
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